ftsH Antibody

Rare Species
Code CSB-PA359465XA01ENV
Size US$299
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  • Western Blot
    Positive WB detected in: recombinant protein
    All lanes:ftsH Antibody at 1:1000
    Secondary
    Goat polyclonal to rabbit IgG at 1/50000 dilution
    Predicted band size: 29.8 kDa
    Observed band size: 30 kDa
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Product Details

Full Product Name
Rabbit anti-Escherichia coli (strain K12) ftsH Antibody Polyclonal antibody
Uniprot No.
Target Names
ftsH Antibody
Alternative Names
ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-) (Cell division protease FtsH) ftsH hflB mrsC std tolZ b3178 JW3145
Raised in
Rabbit
Species Reactivity
Escherichia coli (strain K12)
Immunogen
Recombinant Escherichia coli (strain K12) ftsH protein (141-395aa)
Immunogen Species
Escherichia coli (strain K12)
Conjugate
Non-conjugated
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Tested Applications
ELISA, WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:5000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Usage
For Research Use Only. Not for use in diagnostic or therapeutic procedures.

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Target Background

Function
Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. Degrades a few membrane proteins that have not been assembled into complexes such as SecY, F(0) ATPase subunit a and YccA, and also cytoplasmic proteins sigma-32, LpxC, KdtA and phage lambda cII protein among others. Degrades membrane proteins in a processive manner starting at either the N- or C-terminus; recognition requires a cytoplasmic tail of about 20 residues with no apparent sequence requirements. It presumably dislocates membrane-spanning and periplasmic segments of the protein into the cytoplasm to degrade them, this probably requires ATP. Degrades C-terminal-tagged cytoplasmic proteins which are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (SsrA) stable RNA.; As FtsH regulates the levels of both LpxC and KdtA it is required for synthesis of both the protein and lipid components of lipopolysaccharide (LPS).; (Microbial infection) Probably transports the toxic C-terminal region of CdiA from E.coli strain 536, E.cloacae strain ATCC 13047 and of Y.pestis strain A across the inner membrane to the cytoplasm, where CdiA has a toxic effect. Toxin transport is strain-specific, mutations in this gene do not confer resistance to several other tested CdiA toxins.
Gene References into Functions
  1. FtsH-mediated coordination of lipopolysaccharide biosynthesis correlates with the growth rate. PMID: 23417489
  2. FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm. PMID: 21700705
  3. report the first purification of E. coli HflK and HflC separately as active and functional proteins and show that each can interact with HflB on its own and each inhibits the proteolysis of lambdaCII PMID: 20599668
  4. show that FtsH exists exclusively as a large complex, termed FtsH holo-enzyme, which can be separated from bulk of membrane proteins after detergent solubilization and velocity sedimentation; a tentative model is presented PMID: 15037243
  5. FtsH hexamer degrades approximately 0.5 molecules of Cy3-sigma32 per min at 42 degrees C and hydrolyzes approximately 140 ATP molecules during the degradation of a single molecule of Cy3-sigma32 PMID: 15037246
  6. The in vivo stability of the mutated RpoH proteins correlated with their stability in a purified in vitro degradation system, suggesting that region 2.1 might be directly involved in the interaction with the FtsH protease. PMID: 17660420
  7. The mechanism of lambda CIII inhibition of E. coli HflB was studied. PMID: 17890311
  8. inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 of lambdaCIII) & lack of interaction between sigma(32) & CIII. PMID: 18721134
  9. Data show that FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of LPS. PMID: 18776015
  10. RpoH fragment composed of residues 37-147 is degraded in an FtsH-dependent manner. PMID: 19025566

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Subcellular Location
Cell inner membrane; Multi-pass membrane protein.
Protein Families
AAA ATPase family; Peptidase M41 family
Database Links
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